Characterizations of cross-bridges in the presence of saturating concentrations of MgAMP-PNP in rabbit permeabilized psoas muscle

Biophysical Journal
S M FrisbieL C Yu

Abstract

Several earlier studies have led to different conclusions about the complex of myosin with MgAMP-PNP. It has been suggested that subfragment 1 of myosin (S1)-MgAMP-PNP forms an S1-MgADP-like state, an intermediate between the myosin S1-MgATP and myosin S1-MgADP states or a mixture of cross-bridge states. We suggest that the different states observed result from the failure to saturate S1 with MgAMP-PNP. At saturating MgAMP-PNP, the interaction of myosin S1 with actin is very similar to that which occurs in the presence of MgATP. 1) At 1 degrees C and 170 mM ionic strength the equatorial x-ray diffraction intensity ratio I11/I10 decreased with an increasing MgAMP-PNP concentration and leveled off by approximately 20 mM MgAMP-PNP. The resulting ratio was the same for MgATP-relaxed fibers. 2) The two dimensional x-ray diffraction patterns from MgATP-relaxed and MgAMP-PNP-relaxed bundles are similar. 3) The affinity of S1-MgAMP-PNP for the actin-tropomyosin-troponin complex in solution in the absence of free calcium is comparable with that of S1-MgATP. 4) In the presence of calcium, I11/I10 decreased toward the relaxed value with increasing MgAMP-PNP, signifying that the affinity between cross-bridge and actin is weakened by MgAMP-...Continue Reading

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Citations

May 3, 2002·European Journal of Biochemistry·Nóra HartvigJoseph Belagyi
Jul 22, 1999·Annals of the New York Academy of Sciences·D L Burgess, J L Noebels
Jan 15, 1999·Acta Physiologica Scandinavica·J M ChalovichY D Chen
Jul 19, 2002·Biophysical Journal·Andrea M ResetarJoseph M Chalovich

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